Q62005 · ZP1_MOUSE
- ProteinZona pellucida sperm-binding protein 1
- GeneZp1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids623 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP1 ensures the structural integrity of the zona pellucida.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | egg coat | |
Cellular Component | extracellular region | |
Cellular Component | plasma membrane | |
Molecular Function | structural constituent of egg coat | |
Biological Process | single fertilization |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameZona pellucida sperm-binding protein 1
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ62005
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Processed zona pellucida sperm-binding protein 1
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 21-590 | Extracellular | ||||
Sequence: QRLHLEPGFEYSYDCGVRGMQLLVFPRPNQTVQFKVLDEFGNRFEVNNCSICYHWVTSEAQEHTVFSADYKGCHVLEKDGRFHLRVFIQAVLPNGRVDIAQDVTLICPKPDHTVTPDPYLAPPTTPEPFTPHAFALHPIPDHTLAGSGHTGLTTLYPEQSFIHPTPAPPSLGPGPAGSTVPHSQWGTLEPWELTELDSVGTHLPQERCQVASGHIPCMVNGSSKETCQQAGCCYDSTKEEPCYYGNTVTLQCFKSGYFTLVMSQETALTHGVLLDNVHLAYAPNGCPPTQKTSAFVVFHVPLTLCGTAIQVVGEQLIYENQLVSDIDVQKGPQGSITRDSAFRLHVRCIFNASDFLPIQASIFSPQPPAPVTQSGPLRLELRIATDKTFSSYYQGSDYPLVRLLREPVYVEVRLLQRTDPSLVLVLHQCWATPTTSPFEQPQWPILSDGCPFKGDNYRTQVVAADREALPFWSHYQRFTITTFMLLDSSSQNALRGQVYFFCSASACHPLGSDTCSTTCDSGIARRRRSSGHHNITLRALDIVSSPGAVGFEDAAKLEPSGSSRNSSSRM | ||||||
Transmembrane | 591-611 | Helical | ||||
Sequence: LLLLLAITLALAAGIFVGLIW | ||||||
Topological domain | 612-623 | Cytoplasmic | ||||
Sequence: AWAQKLWEGIRY |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, modified residue, glycosylation, disulfide bond, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MAWGCFVVLLLLAAAPLRLG | ||||||
Chain | PRO_0000304554 | 21-? | Processed zona pellucida sperm-binding protein 1 | |||
Sequence: MAWGCFVVLLLLAAAPLRLG | ||||||
Modified residue | 21 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_0000041679 | 21-546 | Zona pellucida sperm-binding protein 1 | |||
Sequence: QRLHLEPGFEYSYDCGVRGMQLLVFPRPNQTVQFKVLDEFGNRFEVNNCSICYHWVTSEAQEHTVFSADYKGCHVLEKDGRFHLRVFIQAVLPNGRVDIAQDVTLICPKPDHTVTPDPYLAPPTTPEPFTPHAFALHPIPDHTLAGSGHTGLTTLYPEQSFIHPTPAPPSLGPGPAGSTVPHSQWGTLEPWELTELDSVGTHLPQERCQVASGHIPCMVNGSSKETCQQAGCCYDSTKEEPCYYGNTVTLQCFKSGYFTLVMSQETALTHGVLLDNVHLAYAPNGCPPTQKTSAFVVFHVPLTLCGTAIQVVGEQLIYENQLVSDIDVQKGPQGSITRDSAFRLHVRCIFNASDFLPIQASIFSPQPPAPVTQSGPLRLELRIATDKTFSSYYQGSDYPLVRLLREPVYVEVRLLQRTDPSLVLVLHQCWATPTTSPFEQPQWPILSDGCPFKGDNYRTQVVAADREALPFWSHYQRFTITTFMLLDSSSQNALRGQVYFFCSASACHPLGSDTCSTTCDSGIARR | ||||||
Glycosylation | 49 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 68 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 228↔253 | |||||
Sequence: CQVASGHIPCMVNGSSKETCQQAGCC | ||||||
Disulfide bond | 237↔252 | |||||
Sequence: CMVNGSSKETCQQAGC | ||||||
Glycosylation | 240 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 247↔262 | |||||
Sequence: CQQAGCCYDSTKEEPC | ||||||
Glycosylation | 371 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 449↔470 | |||||
Sequence: CWATPTTSPFEQPQWPILSDGC | ||||||
Propeptide | PRO_0000041680 | 547-623 | Removed in mature form | |||
Sequence: RRSSGHHNITLRALDIVSSPGAVGFEDAAKLEPSGSSRNSSSRMLLLLLAITLALAAGIFVGLIWAWAQKLWEGIRY | ||||||
Glycosylation | 554 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 585 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
O-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in oocytes.
Developmental stage
Not detected in resting oocytes. As oocytes begin to grow, levels increase to reach a maximum in midsized oocytes. Levels decrease in later stages of oocyte growth.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 182-201 | Disordered | ||||
Sequence: IHPTPAPPSLGPGPAGSTVP | ||||||
Domain | 226-266 | P-type | ||||
Sequence: ERCQVASGHIPCMVNGSSKETCQQAGCCYDSTKEEPCYYGN | ||||||
Domain | 271-542 | ZP | ||||
Sequence: QCFKSGYFTLVMSQETALTHGVLLDNVHLAYAPNGCPPTQKTSAFVVFHVPLTLCGTAIQVVGEQLIYENQLVSDIDVQKGPQGSITRDSAFRLHVRCIFNASDFLPIQASIFSPQPPAPVTQSGPLRLELRIATDKTFSSYYQGSDYPLVRLLREPVYVEVRLLQRTDPSLVLVLHQCWATPTTSPFEQPQWPILSDGCPFKGDNYRTQVVAADREALPFWSHYQRFTITTFMLLDSSSQNALRGQVYFFCSASACHPLGSDTCSTTCDSG |
Domain
The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.
Sequence similarities
Belongs to the ZP domain family. ZPB subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length623
- Mass (Da)68,723
- Last updated1996-11-01 v1
- Checksum9D95B8613B3B95C8
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F7CW32 | F7CW32_MOUSE | Zp1 | 95 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 246 | in Ref. 1; AAC48480 | ||||
Sequence: T → A | ||||||
Sequence conflict | 445 | in Ref. 1; AAC48480 | ||||
Sequence: V → L | ||||||
Sequence conflict | 486 | in Ref. 1; AAC48480 | ||||
Sequence: R → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U24230 EMBL· GenBank· DDBJ | AAB60507.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U24227 EMBL· GenBank· DDBJ | AAB60507.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U24228 EMBL· GenBank· DDBJ | AAB60507.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U24229 EMBL· GenBank· DDBJ | AAB60507.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U20448 EMBL· GenBank· DDBJ | AAC48480.1 EMBL· GenBank· DDBJ | mRNA |